Functional amyloids in the human body

Amy Brown; Marianna Török

doi:10.1016/j.bmcl.2021.127914

Functional amyloids in the human body

Bioorg Med Chem Lett. 2021 May 15:40:127914. doi: 10.1016/j.bmcl.2021.127914. Epub 2021 Mar 7.

Authors

Amy Brown¹, Marianna Török²

Affiliations

¹ Department of Chemistry, University of Massachusetts Boston, 100 Morrissey Blvd., Boston, MA 02125, USA.
² Department of Chemistry, University of Massachusetts Boston, 100 Morrissey Blvd., Boston, MA 02125, USA. Electronic address: marianna.torok@umb.edu.

PMID: 33691165
DOI: 10.1016/j.bmcl.2021.127914

Abstract

Amyloids have long been associated with a variety of human degenerative diseases. Discoveries indicate, however, that there are several amyloids that serve functional roles in the human body. These amyloids are involved in a variety of biological processes ranging from storage of peptide hormones to necroptosis of cells. Additionally, there are distinct differences between toxic amyloids and their functional counterparts including kinetics of assembly/disassembly and structural features. This digest article surveys the biological roles of functional amyloids found in the human body, key differences between functional and toxic amyloids, and potential therapeutic applications.

Keywords: Amyloid; Drug delivery; Hormone; Peptide; Self-assembly.

Publication types

Review

MeSH terms

Amyloid / chemistry*
Amyloid / metabolism*
Animals
Hormones / metabolism
Human Body
Humans
Kinetics
Neurodegenerative Diseases / physiopathology*
Neurodegenerative Diseases / therapy*
Nuclear Pore Complex Proteins / metabolism
Peptides / chemistry
Protein Aggregates / physiology
Protein Conformation
RNA-Binding Proteins / metabolism
Receptor-Interacting Protein Serine-Threonine Kinases / metabolism
Signal Transduction

Substances

AGFG1 protein, human
Amyloid
Hormones
Nuclear Pore Complex Proteins
Peptides
Protein Aggregates
RNA-Binding Proteins
RIPK3 protein, human
Receptor-Interacting Protein Serine-Threonine Kinases